ID A0A1D7MU54_BIFLN Unreviewed; 917 AA. AC A0A1D7MU54; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 25-APR-2018, entry version 16. DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|HAMAP-Rule:MF_00097}; DE Includes: DE RecName: Full=Phosphomethylpyrimidine synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE EC=4.1.99.17 {ECO:0000256|HAMAP-Rule:MF_00089}; DE AltName: Full=Hydroxymethylpyrimidine phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE AltName: Full=Thiamine biosynthesis protein ThiC {ECO:0000256|HAMAP-Rule:MF_00089}; DE Short=HMP-P synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE Short=HMP-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE Short=HMPP synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE Includes: DE RecName: Full=Thiamine-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00097}; DE Short=TP synthase {ECO:0000256|HAMAP-Rule:MF_00097}; DE Short=TPS {ECO:0000256|HAMAP-Rule:MF_00097}; DE EC=2.5.1.3 {ECO:0000256|HAMAP-Rule:MF_00097}; DE AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00097}; DE Short=TMP pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00097}; DE Short=TMP-PPase {ECO:0000256|HAMAP-Rule:MF_00097}; GN Name=thiE {ECO:0000256|HAMAP-Rule:MF_00097}; GN Synonyms=thiC {ECO:0000256|HAMAP-Rule:MF_00089}; GN ORFNames=APC1462_1376 {ECO:0000313|EMBL:PKD11236.1}, APC1503_1426 GN {ECO:0000313|EMBL:PKC88078.1}, B624_1208 GN {ECO:0000313|EMBL:AOL10665.1}, CYJ39_05960 GN {ECO:0000313|EMBL:PKY76853.1}; OS Bifidobacterium longum. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=216816 {ECO:0000313|EMBL:AOL10665.1, ECO:0000313|Proteomes:UP000094138}; RN [1] {ECO:0000313|EMBL:AOL10665.1, ECO:0000313|Proteomes:UP000094138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=35624 {ECO:0000313|EMBL:AOL10665.1, RC ECO:0000313|Proteomes:UP000094138}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AOL10665.1, ECO:0000313|Proteomes:UP000094138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=35624 {ECO:0000313|EMBL:AOL10665.1, RC ECO:0000313|Proteomes:UP000094138}; RA van Sinderen D., O' Mahoney L.; RT "Genome analysis and characterisation of the surface-associated RT exopolysaccharide produced by Bifidobacterium longum subsp. longum RT 35624TM."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:PKC88078.1, ECO:0000313|Proteomes:UP000232439, ECO:0000313|Proteomes:UP000232654} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APC1462 {ECO:0000313|EMBL:PKD11236.1, RC ECO:0000313|Proteomes:UP000232439}, and APC1503 RC {ECO:0000313|EMBL:PKC88078.1, ECO:0000313|Proteomes:UP000232654}; RA Arboleya S.; RT "Bifidobacterium longum APC/DPC strains."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:PKY76853.1, ECO:0000313|Proteomes:UP000234964} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UMB0788 {ECO:0000313|EMBL:PKY76853.1, RC ECO:0000313|Proteomes:UP000234964}; RA Thomas-White K., Wolfe A.J.; RT "Phylogenetic diversity of female urinary microbiome."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction. {ECO:0000256|HAMAP-Rule:MF_00089, CC ECO:0000256|SAAS:SAAS00956671}. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP). {ECO:0000256|HAMAP-Rule:MF_00097, CC ECO:0000256|SAAS:SAAS00709677}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate CC = diphosphate + thiamine phosphate + CO(2). {ECO:0000256|HAMAP- CC Rule:MF_00097, ECO:0000256|SAAS:SAAS00709728}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate = diphosphate + CC thiamine phosphate + CO(2). {ECO:0000256|HAMAP-Rule:MF_00097, CC ECO:0000256|SAAS:SAAS00709678}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine CC phosphate. {ECO:0000256|HAMAP-Rule:MF_00097, CC ECO:0000256|SAAS:SAAS00709726}. CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5- CC (phosphomethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + CC formate + CO. {ECO:0000256|HAMAP-Rule:MF_00089, CC ECO:0000256|SAAS:SAAS00956665}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00097}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00097}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00097, CC ECO:0000256|SAAS:SAAS00709682}. CC -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000256|HAMAP- CC Rule:MF_00089, ECO:0000256|SAAS:SAAS00976596}. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC {ECO:0000256|HAMAP-Rule:MF_00097}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP013673; AOL10665.1; -; Genomic_DNA. DR EMBL; PJDT01000021; PKC88078.1; -; Genomic_DNA. DR EMBL; PJEF01000011; PKD11236.1; -; Genomic_DNA. DR EMBL; PKGP01000005; PKY76853.1; -; Genomic_DNA. DR RefSeq; WP_011067965.1; NZ_PJEF01000011.1. DR EnsemblBacteria; AOL10665; AOL10665; B624_1208. DR PATRIC; fig|216816.126.peg.1287; -. DR UniPathway; UPA00060; UER00141. DR Proteomes; UP000094138; Chromosome. DR Proteomes; UP000232439; Unassembled WGS sequence. DR Proteomes; UP000232654; Unassembled WGS sequence. DR Proteomes; UP000234964; Unassembled WGS sequence. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd00564; TMP_TenI; 1. DR Gene3D; 3.20.20.540; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR036206; ThiamineP_synth_sf. DR InterPro; IPR022998; ThiamineP_synth_TenI. DR InterPro; IPR037509; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR038521; ThiC/Bza_sf. DR InterPro; IPR002817; ThiC/BzaA/B. DR InterPro; IPR034291; TMP_synthase. DR PANTHER; PTHR30557; PTHR30557; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF01964; ThiC_Rad_SAM; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SFLD; SFLDF00407; phosphomethylpyrimidine_syntha; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00089, KW ECO:0000256|SAAS:SAAS00923200}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000094138, KW ECO:0000313|Proteomes:UP000232439, ECO:0000313|Proteomes:UP000232654, KW ECO:0000313|Proteomes:UP000234964}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|SAAS:SAAS00923199}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00089, KW ECO:0000256|SAAS:SAAS00923226}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00089, KW ECO:0000256|SAAS:SAAS00923244}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00097, KW ECO:0000256|SAAS:SAAS00709725}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00089, KW ECO:0000256|SAAS:SAAS00923246}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00089, KW ECO:0000256|SAAS:SAAS00923219}; KW Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00089, KW ECO:0000256|SAAS:SAAS00956670}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00097, KW ECO:0000256|SAAS:SAAS00709679, ECO:0000313|EMBL:PKY76853.1}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|SAAS:SAAS00923206}. FT DOMAIN 19 219 TMP-TENI. {ECO:0000259|Pfam:PF02581}. FT DOMAIN 327 381 ThiC-associated. {ECO:0000259|Pfam: FT PF13667}. FT REGION 48 52 HMP-PP binding. {ECO:0000256|HAMAP-Rule: FT MF_00097}. FT REGION 157 159 THZ-P binding. {ECO:0000256|HAMAP-Rule: FT MF_00097}. FT REGION 216 217 THZ-P binding. {ECO:0000256|HAMAP-Rule: FT MF_00097}. FT REGION 601 603 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00089}. FT REGION 642 645 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00089}. FT COILED 380 400 {ECO:0000256|SAM:Coils}. FT METAL 85 85 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00097}. FT METAL 109 109 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00097}. FT METAL 685 685 Zinc. {ECO:0000256|HAMAP-Rule:MF_00089}. FT METAL 749 749 Zinc. {ECO:0000256|HAMAP-Rule:MF_00089}. FT METAL 829 829 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_00089}. FT METAL 832 832 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_00089}. FT METAL 837 837 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_00089}. FT BINDING 84 84 HMP-PP. {ECO:0000256|HAMAP-Rule: FT MF_00097}. FT BINDING 128 128 HMP-PP. {ECO:0000256|HAMAP-Rule: FT MF_00097}. FT BINDING 160 160 HMP-PP. {ECO:0000256|HAMAP-Rule: FT MF_00097}. FT BINDING 196 196 THZ-P; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00097}. FT BINDING 487 487 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00089}. FT BINDING 516 516 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00089}. FT BINDING 545 545 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00089}. FT BINDING 581 581 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00089}. FT BINDING 681 681 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00089}. FT BINDING 708 708 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00089}. SQ SEQUENCE 917 AA; 100355 MW; 00000DA28A98E1F6 CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAMLADTKA AGWFVVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVTHTPATDT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LATAKANVDN GVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE //